Evidence map›Paper›PMID 26549102›Full record

ArticleNature communications2015

X-ray structure and activities of an essential Mononegavirales L-protein domain.

Guido C Paesen, Axelle Collet, Corinne Sallamand, Françoise Debart, Jean-Jacques Vasseur, Bruno Canard, Etienne Decroly, Jonathan M Grimes

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 72 citations in OpenAlex.

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  8. Structural insights into the dynamic mechanism of bornavirus polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  18. Methyltransferases ofBiomolecules · 2022
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Guido C PaesenDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, Oxford OX3 7BN, UK.
Axelle ColletAFMB, CNRS, Aix-Marseille University, UMR 7257, Case 925, 163 Avenue de Luminy, 13288 Marseille, France.
Corinne SallamandDepartment of Nucleic Acids, IBMM, UMR 5247, CNRS, Université Montpellier, ENSCM, Campus Triolet, Place E. Bataillon, 34095 Montpellier, France.
Françoise DebartDepartment of Nucleic Acids, IBMM, UMR 5247, CNRS, Université Montpellier, ENSCM, Campus Triolet, Place E. Bataillon, 34095 Montpellier, France.
Jean-Jacques VasseurDepartment of Nucleic Acids, IBMM, UMR 5247, CNRS, Université Montpellier, ENSCM, Campus Triolet, Place E. Bataillon, 34095 Montpellier, France.
Bruno CanardAFMB, CNRS, Aix-Marseille University, UMR 7257, Case 925, 163 Avenue de Luminy, 13288 Marseille, France.
Etienne DecrolyAFMB, CNRS, Aix-Marseille University, UMR 7257, Case 925, 163 Avenue de Luminy, 13288 Marseille, France.
Jonathan M GrimesDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, Oxford OX3 7BN, UK.
Centre National de la Recherche Scientifique · FRÉcole Nationale Supérieure de Chimie de Montpellier · FRCentre for Human Genetics · GBDiamond Light Source · GB

Funding

Medical Research Council MR/L017709/1Wellcome Trust 075491/Z/04Wellcome Trust 088190Wellcome Trust 090532
6 · The paper itself

Abstract

The L protein of mononegaviruses harbours all catalytic activities for genome replication and transcription. It contains six conserved domains (CR-I to -VI; Fig. 1a). CR-III has been linked to polymerase and polyadenylation activity, CR-V to mRNA capping and CR-VI to cap methylation. However, how these activities are choreographed is poorly understood. Here we present the 2.2-Å X-ray structure and activities of CR-VI+, a portion of human Metapneumovirus L consisting of CR-VI and the poorly conserved region at its C terminus, the +domain. The CR-VI domain has a methyltransferase fold, which besides the typical S-adenosylmethionine-binding site ((SAM)P) also contains a novel pocket ((NS)P) that can accommodate a nucleoside. CR-VI lacks an obvious cap-binding site, and the (SAM)P-adjoining site holding the nucleotides undergoing methylation ((SUB)P) is unusually narrow because of the overhanging +domain. CR-VI+ sequentially methylates caps at their 2'O and N7 positions, and also displays nucleotide triphosphatase activity.

Indexed as

AnimalsBinding SitesChromatography, Thin LayerCrystallizationCrystallography, X-RayMetapneumovirusMethylationMononegaviralesProtein Structure, TertiaryRNARNA CapsRNA-Dependent RNA PolymeraseS-AdenosylmethionineSf9 CellsSpodopteraViral ProteinsRNARNA CapsRNA-Dependent RNA PolymeraseS-AdenosylmethionineViral Proteins

Identifiers

PMID26549102
PMCPMC4659945
OpenAlexW2191153568

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.